title: Xlr1 is involved in the transcriptional control of the pentose catabolic pathway, but not hemi-cellulolytic enzymes in Magnaporthe oryzae.
abstract: Magnaporthe oryzae is a fungal plant pathogen of many grasses including rice. Since arabinoxylan is one of the major components of the plant cell wall of grasses, M. oryzae is likely to degrade this polysaccharide for supporting its growth in infected leaves. D-Xylose is released from arabinoxylan by fungal depolymerising enzymes and catabolized through the pentose pathway. The expression of genes involved in these pathways is under control of the transcriptional activator XlnR/Xlr1, conserved among filamentous ascomycetes. In this study, we identified M. oryzae genes involved in the pentose catabolic pathway (PCP) and their function during infection, including the XlnR homolog, XLR1, through the phenotypic analysis of targeted null mutants. Growth of the Δxlr1 strain was reduced on D-xylose and xylan, but unaffected on L-arabinose and arabinan. A strong reduction of PCP gene expression was observed in the Δxlr1 strain on D-xylose and L-arabinose. However, there was no significant difference in xylanolytic and cellulolytic enzyme activities between the Δxlr1 mutant and the reference strain. These data demonstrate that XLR1 encodes the transcriptional activator of the PCP in M. oryzae, but does not appear to play a role in the regulation of the (hemi-) cellulolytic system in this fungus. This indicates only partial similarity in function between Xlr1 and A. niger XlnR. The deletion mutant of D-xylulose kinase encoding gene (XKI1) is clearly unable to grow on either D-xylose or L-arabinose and showed reduced growth on xylitol, L-arabitol and xylan. Δxki1 displayed an interesting molecular phenotype as it over-expressed other PCP genes as well as genes encoding (hemi-) cellulolytic enzymes. However, neither Δxlr1 nor Δxki1 showed significant differences in their pathogeny on rice and barley compared to the wild type, suggesting that D-xylose catabolism is not required for fungal growth in infected leaves.
authors.affiliation: Microbiology and Kluyver Centre for Genomics of Industrial Fermentation, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
authors.forename: Evy
authors.initials: E
authors.lastname: Battaglia
authors.forename: Sylvia
authors.initials: S
authors.lastname: Klaubauf
authors.forename: Julie
authors.initials: J
authors.lastname: Vallet
authors.forename: Cecile
authors.initials: C
authors.lastname: Ribot
authors.forename: Marc-Henri
authors.initials: MH
authors.lastname: Lebrun
authors.forename: Ronald P
authors.initials: RP
authors.lastname: de Vries
mesh_terms: D001089:Arabinose / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D020082:Magnaporthe / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D053858:Metabolic Networks and Pathways; D012275:Oryza / Q000382:microbiology; D010429:Pentoses / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics; D014158:Transcription, Genetic; D014990:Xylans / Q000378:metabolism; D014994:Xylose / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D010429:Pentoses; D014990:Xylans; C085118:arabinoxylan; D014994:Xylose; D001089:Arabinose; D017853:Phosphotransferases (Alcohol Group Acceptor); C032700:xylulokinase
keywords: Arabinoxylan; Hemicellulose degradation; Magnaporthe oryzae; Pentose catabolism; XlnR; Xylanase regulator